The epidermal growth factor (EGF) receptor is a 170 kD transmembrane tyrosine kinase and member of the HER/ErbB protein family. Ligand binding results in receptor dimerization, autophosphorylation, activation of downstream signaling and lysosomal degradation (1,2). The SH2 domain of PLC-g binds at phospho-Tyr992, resulting in activation of PLC-g-mediated downstream signaling (6). Phosphorylation of Tyr1045 creates a major docking site for c-Cbl, an adaptor protein that leads to receptor ubiquitination and degradation following EGFR activation (7,8). The GRB2 adaptor protein binds activated EGFR at phospho-Tyr1068 (9). A pair of phosphorylated residues (Tyr1148 and Tyr1173) provide a docking site for the SHC scaffold protein, with both sites involved in MAP kinase signaling activation (2). Phosphorylation of EGFR at specific serine and threonine residues attenuates EGFR kinase activity. EGFR carboxy-terminal residues Ser1046 and Ser1047 are phosphorylated by CaM kinase II; mutations to either of these serines upregulate EGFR tyrosine autokinase activity (10).
Recommended Dilution:Western Blot: 1:1000 Optimal dilutions to be determined by the researcher.
Storage and Stabiity:May be stored at 4°C for short-term only. For long-term storage, aliquot and store at -20°C. Aliquots are stable for 6 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
仕様
Size：1Kit
Grade：Affinity Purified
Purity：Purified by Protein A and peptide affinity chromatography.
Form：Supplied as a liquid in 10mM sodium HEPES, pH 7.5, 150mM sodium chloride, 0.1mg/ml BSA, 50% glycerol.
Specificity：Each phospho-EGF receptor antibody recognizes only the specific phosphorylated form of EGF receptor.
Immunogen：Synthetic phospho-peptides corresponding to residues surrounding Tyr992, Tyr1045 or Tyr1068 of human EGF receptor, respectively.
